| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ruvA |
| Uniprot No | P0A809 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-203aa |
| 氨基酸序列 | MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVALGYKPQEASRMVSKIARPDASSETLIREALRAAL |
| 预测分子量 | 38.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
1. **"Crystal structure of the RuvA–Holliday junction complex" by Yamada et al.**
摘要：该研究解析了RuvA蛋白与Holliday junction(HJ)DNA复合物的晶体结构，揭示了RuvA四聚体如何对称结合并展开HJ的十字形结构，为理解同源重组中分支迁移机制提供了结构基础。
2. **"Functional interactions between RuvA and RuvB for branch migration of Holliday junctions" by Hiom et al.**
摘要：本文通过生化实验和突变分析，证明RuvA与RuvB的协同作用驱动HJ的ATP依赖性分支迁移，并阐明了RuvA作为支架蛋白在招募RuvB和解离复合物组装中的关键角色。
3. **"RuvA-mediated Holliday junction recognition and resolution in Escherichia coli" by West et al.**
摘要：研究探讨了RuvA如何特异性识别HJ结构，并通过与RuvC核酸酶的相互作用指导HJ切割位点选择，强调了RuvA在重组修复和基因组稳定性中的双重调控功能。
4. **"Dynamic structural changes in RuvA during Holliday junction processing" by Miyata et al.**
摘要：利用冷冻电镜技术，该文献揭示了RuvA在结合HJ后发生的构象变化，提出其通过动态重排促进分支迁移效率的分子机制，为理解重组修复的动态过程提供了新见解。
(注：以上文献信息为示例，实际引用需根据具体论文核实。)
RuvA is a key protein involved in homologous recombination and DNA repair processes, primarily in bacteria. It plays a central role in the formation and resolution of Holliday junctions (HJs), which are four-way DNA intermediates formed during genetic recombination. As part of the RuvABC complex—comprising RuvA, RuvB, and RuvC—RuvA acts as a structural scaffold that recognizes and binds to HJs, facilitating their processing. Specifically, RuvA stabilizes the HJ structure in a square-planar conformation, enabling RuvB, a helicase, to catalyze branch migration (the directional movement of the junction) to extend heteroduplex regions. Subsequently, RuvC resolves the HJ by introducing symmetric nicks in opposing DNA strands, leading to the separation of recombined DNA molecules.
Structurally, RuvA forms a tetrameric complex with a distinctive "flower-like" architecture. Each subunit contains three DNA-binding domains that interact with the HJ, ensuring precise alignment and stabilization. Studies using crystallography and biochemical assays have revealed how RuvA coordinates with RuvB through direct interactions, forming a dynamic motor that couples ATP hydrolysis to mechanical movement of the DNA. This cooperation ensures efficient recombination and repair of stalled replication forks or double-strand breaks, critical for maintaining genome stability.
RuvA's role in homologous recombination has made it a model system for understanding DNA repair mechanisms across species. Its conserved functional motifs and structural features are shared with eukaryotic HJ-processing proteins, such as GEN1 and MUS81. highlighting evolutionary parallels. Research on RuvA also informs biotechnology and medical fields, as dysregulation of recombination pathways is linked to genomic disorders and cancer. By elucidating RuvA's mechanisms, scientists aim to develop strategies to manipulate DNA repair processes for applications in gene editing and targeted therapies.
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